Đang chuẩn bị liên kết để tải về tài liệu:
Báo cáo y học: "Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Retrovirology Research cung cấp cho các bạn kiến thức về ngành y đề tài:"Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA. | Retrovirology BioMed Central Research Intracellular interactions between APOBEC3G RNA and HIV-1 Gag APOBEC3G multimerization is dependent on its association with RNA Yeshitila N Friew Vitaly Boyko Wei-Shau Hu and Vinay K Pathak Open Access Address HIV Drug Resistance Program National Cancer Institute-Frederick Frederick Maryland 21702-1201 USA Email Yeshitila N Friew - yfriew@ncifcrf.gov Vitaly Boyko - vb@ncifcrf.gov Wei-Shau Hu - whu@ncifcrf.gov Vinay K Pathak - vpathak@ncifcrf.gov Corresponding author Published 4 June 2009 Received I March 2009 Retrovirology 2009 6 56 doi 10.1186 1742-4690-6-56 Accepted 4 June 2009 This article is available from http www.retrovirology.com content 6 I 56 2009 Friew et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.Org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Host restriction factor APOBEC3G A3G blocks human immunodeficiency virus type 1 HIV-1 replication by G-to-A hypermutation and by inhibiting DNA synthesis and provirus formation. Previous reports have suggested that A3G is a dimer and its virion incorporation is mediated through interactions with viral or nonviral RNAs and or HIV-1 Gag. We have now employed a bimolecular fluorescence complementation assay BiFC to analyze the intracellular A3G-A3G A3G-RNA and A3G-Gag interactions in living cells by reconstitution of yellow fluorescent protein YFP from its N- or C-terminal fragments. Results The results obtained with catalytic domain 1 and 2 CD1 and CD2 mutants indicate that A3G-A3G and A3G-Gag multimerization is dependent on an intact CD1 domain which is required for RNA binding. A mutant HIV-1 Gag that exhibits reduced RNA binding also failed to reconstitute BiFC with wild-type A3G indicating a requirement for both HIV-1 Gag and A3G to bind to RNA for their